MolNFT v1 · #142557 · protein
Crystal structure of the C-terminal periplasmic domain of eceptc from escherichia COLI complex with zn
6A83 · Phosphoethanolamine transferase eptc: “Crystal structure of the C-terminal periplasmic domain of eceptc from escherichia COLI complex with zn”. X-ray diffraction, 2 ligands (ZN, NA), 3 pockets (best druggability 0.50). MolNFT v1…
- PDB
- 6A83
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoethanolamine transferase eptc
- EC
- 2.7.-.-
- UniProt
- P0CB39
- Ligands
- ZN, NA
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoethanolamine transferase eptc (EC 2.7.-.-) | protein | 357 | 33% helix, 17% strand | P0CB39 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.50 | 0.86 | 19 | empty |
| 2 | 158 | 0.47 | 0.77 | 24 | empty |
| 3 | 81 | 0.37 | 0.77 | 15 | empty |
Compared structures
- 6A83 · Crystal structure of the C-terminal periplasmic domain of EcEptC from Escherichia coli… · the same entry in another collection · chain A against A, TM-score 1.00
- P0CB39 · AlphaFold monomer V2.0 prediction for phosphoethanolamine transferase eptc (P0CB39) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0CB39
- Elsewhere: RCSB PDB 6A83 · PDBe 6A83 · UniProt P0CB39
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